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. 2001 Mar 15;20(6):1469–1476. doi: 10.1093/emboj/20.6.1469

graphic file with name cde139f5.jpg

Fig. 5. A model describing the DnaA-dependent unwinding reaction at oriC. The DnaA box R1 and the three 13mers are labeled. The six ATP-DnaA boxes are indicated by small gray boxes. Initially, DnaA protein binds with a high affinity to DnaA box R1. This complex serves as an anchor for cooperative binding of ATP-DnaA to the ATP-DnaA boxes, positioning the protein to the region of unwinding. The formation of this complex needs high concentrations of ATP-DnaA protein and can be considered, therefore, as the rate-limiting reaction in unwinding. Single-stranded DNA resulting from unwinding will then be stabilized by cooperative binding of ATP-DnaA. The affinity of ATP-DnaA is higher to single-stranded ATP-DnaA boxes than to double-stranded ATP-DnaA boxes.